Recombinant Human CES1G protein

CES1G (carboxylesterase 1G) is a splice variant of the CES1 gene, which encodes a serine hydrolase involved in the metabolism of xenobiotics and endogenous lipids. As a member of the carboxylesterase family, CES1G shares structural homology with CES1A, the predominant isoform, but differs in its C-terminal region due to alternative splicing. This enzyme is primarily expressed in the liver and plays a critical role in hydrolyzing ester-containing compounds, including prodrugs (e.g., antiviral agents), environmental toxins, and lipid-derived signaling molecules. Its catalytic triad (Ser-221. Glu-354. His-468) and conserved α/β-hydrolase fold enable substrate recognition and hydrolysis.

Recombinant CES1G protein is produced using expression systems like Escherichia coli or mammalian cells for functional studies. Researchers utilize it to investigate substrate specificity, enzyme kinetics, and inhibition mechanisms, often comparing its activity with CES1A to elucidate isoform-specific roles. Notably, CES1G exhibits altered catalytic efficiency toward certain substrates (e.g., clopidogrel) due to structural variations, highlighting its unique pharmacological relevance. It also shows potential in drug development, particularly in optimizing prodrug activation or detoxification pathways.

Recent studies explore CES1G's involvement in metabolic disorders and cancers, as dysregulation of lipid metabolism may link its activity to disease progression. However, challenges remain in characterizing its endogenous substrates and regulatory mechanisms. Recombinant CES1G serves as a vital tool for advancing precision medicine, enabling targeted therapies that account for interindividual variability in drug metabolism. Ongoing research aims to clarify its physiological roles and therapeutic applications, leveraging structural biology and high-throughput screening approaches.